Publication details

Galectin-like protein from Ralstonia solanacearum

Authors

ŠULÁK Ondřej KOSTLÁNOVÁ Nikola MITCHELL Edvard IMBERTY Anne WIMMEROVÁ Michaela

Year of publication 2007
Type Article in Proceedings
Conference Current chemistry and biochemistry of saccharides - Cukrblik 2007
MU Faculty or unit

Faculty of Science

Citation
Field Biochemistry
Keywords Ralstonia solanacearum - lectin
Description Ralstonia solanacearum is a Gram-negative bacterial pathogen that causes several diseases in a wide range of plants (tomatoes, peppers, eggplant, banana etc.) [1]. Lectins are carbohydrate-binding proteins or glycoproteins, which are highly specific for their sugar moieties in cell walls or membranes and thereby change the physiology of the membrane. Lectins are known for their ability to agglutinate erythrocytes in vitro. Plant and animal pathogens use these protein-carbohydrate interactions in their strategy for host recognition and invasion. Since there are not any known treatments of resistant plant species, identifying target molecules for the bacterium in host plants could help to develop a strategy against its infection. As far as we know, the R. solanacearum bacterium has been producing three soluble lectins, RSL (9.9 kDa) [2], RS-IIL (11.6 kDa) [3] and newly discovered RS20L (20 kDa) This contribution structurally and functionally describes RS20L, which has no sequence similarity to any known amino acid sequence. Although resolution of crystal structure showed high structural similarity to animal galectins, it does not display sugar specifity to D-galactose.
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